Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0019163 (hepatitis B)
 38,309 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Renal disorders complicating liver disease are a frequent finding. Extrahepatic causes like intoxications and circulatory dysfunction or diseases that simultaneously affect both the liver and the kidney, like multisystem or viral diseases (hepatitis B) have to be differentiated from clinical entities in which, like in liver cirrhosis or in fulminant hepatitis, the manifestation of renal disease has to be understood as a consequence of the hepatic disorders. Functional disturbances like the increases in tubular sodium reabsorption or the hepatorenal syndrome have been thoroughly investigate because of their clinical importance. Substantial research dealing with the consequences of the increased intrahepatic vascular resistance on systemic and renal hemodynamics and with vasoactive substances, either arising from the liver or accumulating due to poor inactivation by the liver, have led - in the last years - to a better understanding of the pathophysiology of renal involvement in liver disease. However, the exact pathophysiologic role of factors like the effective blood volume, the sympathoadrenergic tonus, the activation of the renin-angiotensin-aldosterone system, changes of kinin activity or in prostaglandin release and the accumulation of "false" neurotransmitters and endotoxins still remains to be established.
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PMID:[Kidney involvement in liver diseases. Pathophysiology and clinical course]. 664 4

Onchocerca supernatant (OS) was prepared by a technique permitting live microfilariae to migrate from nodule tissue through agar gel into sterile Hanks balanced salt/Penicillin-Streptomycin solution where they metabolized. The OS, after dialysis, was passed through Seitz viral filter and either concentrated or lyophilized. Using rabbit antiserum in immunodiffusion and immunoelectrophoresis tests, microfilariae proteins and also human protein were detected in out OS. No common antigens were found between this and somatic extracts of Loa loa, O. gutturosa, O. volvulus, L. carinii, D. immittis and A. lumbricoides. 125I labelled OS was purified by passage through protein A column and then through immunosorbent column of horse anti-human serum linked to CNB-activated sepharose 4B. Autoradiography, after sodium dodecyl sulphate polyacylamide slab gel eletrophoresis of purified OS, showed 10 protein bands in the molecular range 10,000 to 125,000. Skin prick tests with OS, shown not to be contaminated with Hepatitis B antigens, elicited immediate hypersensitivity reaction. Using our criteria, positive reactions were seen in 81% of proven onchocerca cases and only occasionally in Loasis 4.5%, ascaridiasis 13.5% or healthy controls 2.4%. The poor skin reactivity to OS in loasis was not due to immunosuppression as these patients, when also infested with ascaris, reacted just as well as onchocerca patients with ascaris to skin prick test using somatic extracts of ascaris.
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PMID:A diagnostic skin test for Onchocerca volvulus infection. 680 26

Three hepatitis B surface antigen (HBsAg) preparations were compared: purified intact 22-nm HBsAg particles; HBsAg-derived, sodium dodecyl sulfate (SDS)-denatured P25 + GP30 polypeptide pool; and nondenatured P25 + GP30 micelles. The micelles had the same polypeptide composition as the P25 + GP30 pool. The immunogenicity in mice of each preparation, administered either in saline suspension or adsorbed to aluminum gel, was compared. The SDS-denatured polypeptides were less immunogenic than intact HBsAg particles, whereas the micelles were more immunogenic. High anti-HBs titers were observed in mice immunized with micelle preparations in either saline suspension or adsorbed to aluminum gel for as long as 200 days after a booster inoculation, administered 26 days after the primary dose.
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PMID:Comparative studies of the immunogenic activity of hepatitis B surface antigen (HBsAg) and HBsAg polypeptides. 684 90

Using a monoclonal IgM antibody (anti-HBs) to hepatitis B surface antigen (HBsAg) in a radioimmunoassay for hepatitis B, we have detected high binding activity in human serum that was unreactive in assays employing conventional anti-HBs reagents. The binding material was isolated from serum by affinity chromatography on monoclonal IgM anti-HBs, and comparison of the material with HBsAg (by sodium dodecyl sulfate/polyacrylamide gel electrophoresis) demonstrated that the two shared several similar polypeptides. Furthermore, comparison of the binding properties of HBsAg and concentrated monoclonal immunoreactive material with conventional and monoclonal anti-HBs reagents demonstrated some antigenic crossreactivity. The molecular weight of the monoclonal immunoreactive material was approximately 2 X 10(6). Immunoprecipitation of the material with monoclonal IgM antibodies and examination by electron microscopy revealed clumped and "spiculated" particles that resembled 22-nm hepatitis B particles coated with the same antibody. Thus, this study suggests that the high-binding-activity material, detected in serum only by the monoclonal radioimmunoassay, is not identical with HBsAg, but it shares some common properties.
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PMID:Monoclonal IgM radioimmunoassay for hepatitis B surface antigen: high binding activity in serum that is unreactive with conventional antibodies. 695 Nov 73

Hepatitis B surface antigens (HBsAg) of both the adw and ayw subtypes have been purified from four different sources. These antigens have been compared by comparison of the products of tryptic hydrolysis performed under conditions which do not disrupt the overall particle morphology of HBsAg. The resultant peptides were compared by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and high performance liquid chromatography followed by amino acid analysis and Edman degradation of the isolated peptides. The same techniques were also applied to HBsAg which had been labeled with tritium in the carbohydrate moiety of the glycoprotein gp-30. These studies demonstrate that residues 122-150 of the protein p-25 and glycoprotein gp-30 occupy an exposed region of the HBsAg lipoprotein particle and contain the major attachment site for carbohydrate in the case of gp-30. The two subtypes were found to differ at two specific positions in this region, suggesting that this is an antigenically important area of the protein.
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PMID:Structure of hepatitis B surface antigen. Correlation of subtype with amino acid sequence and location of the carbohydrate moiety. 710 12

The relationships among the core antigen polypeptides of hepatitis B virus (HBV) and ground squirrel hepatitis virus (GSHV) were studied using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and tryptic peptide mapping. The major core antigen polypeptides of liver-derived HBV (p22) and GSHV (p20.5) shared 56% of the spots in their peptide maps. Comparison of hepatitis B core antigen (HBcAg) p19 or ground squirrel hepatitis core antigen (GSHcAg) p16.5 with their respective major polypeptides indicated that these components probably resulted from cleavage of the major polypeptide of each virus. Other polypeptides smaller than the major component of each virus were often faint on polyacrylamide gels and probably resulted from the cleavage or degradation of components larger than p22 of HBcAg or p20.5 of GSHcAg, since their peptide maps contained spots unique to these high-molecular-weight components. p26 of GSHcAg and p27.5 of HBcAg shared approximately two-thirds of the spots on their peptide maps with those of their respective major core polypeptides. Furthermore, p37.5 of GSHcAg and p40 of HBcAg shared about 60% homology with their respective major polypeptides, and also shared many of the spots that were unique to p26 of GSHcAg or p27.5 of HBcAg but were not found in the peptide map of their respective core antigen polypeptides. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis bands larger than 40,000 daltons were variably present, and peptide mapping indicated that these were aggregates of various smaller core antigen-associated polypeptides. The results suggest that p40 of HBcAg and p37.5 of GSHcAg are the largest unique polypeptides in these core particles, and that they are encoded for by the genome of each virus. That a subset of the spots unique to p40 or p37.5 was also found in p27.5 of HBcAg or p26 of GSHcAg, respectively, as compared to the major core polypeptides, also suggests that p27.5 and p26 are unique proteins encoded by the genome of each virus. It is proposed that the core antigen gene of each virus is larger than that which would encode the major polypeptide of each virus, and that the genetic organizations of the core genes of HBV and GSHV are very similar.
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PMID:Core particles of hepatitis B virus and ground squirrel hepatitis virus. I. Relationship between hepatitis B core antigen- and ground squirrel hepatitis core antigen-associated polypeptides by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and tryptic peptide mapping. 710 37

The effects of heat, sodium hypochlorite, diethyl ether, and ethyl alcohol on the activity of DNA polymerase (DNA-P) associated with hepatitis B virsus (HBV) in serum were evaluated. The response of DNA-P to heating at 60 degrees C for 15, 30, 45, 60, 90, 120, 180, and 240 minutes was studied and the data suggested that there may be two types of DNA-P. The majority of DNA-P was type 'a', and it showed a one log reduction (D60) at 60 degrees C in 36 minutes, while the remaining activity was type 'b' that showed a one log reduction (D60) in 340 minutes. Treatment of DNA-P with sodium hypochlorite at concentrations of 250 and 500 parts per million (ppm) of available chlorine resulted in a 20 to 25% reduction in DNA-P activity within one minute. Complete loss in detectable DNA-P activity occurred within one minute when available Cl- was 2500 ppm or greater. Various concentrations of ethyl alcohol (ranging from 10 to 70%) caused gradually increasing inactivation of DNA-P activity in ten minutes at 4 degrees C. Ninety percent inactivation occurred with 60% alcohol. Overnight treatment of DNA-P-reactive material with diethyl ether at 4 degrees C led to loss of detectable activity. A reduction in the titer of HBsAg was found following treatment with alcohol or ether. The possible use of DNA-P assay as an indicator of the rate of inactivation of HBV is proposed.
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PMID:Inactivation of DNA-polymerase associated with hepatitis B virus. 714 78

Hepatitis B surface antigen has been purified and its major protein (p-25) and glycoprotein (gp-30) isolated. These isolated proteins have been subjected to amino acid analysis, Edman degradation (30 steps), carboxypeptidase digestion, and peptide mapping following tryptic hydrolysis by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, two-dimensional thin layer chromatography and electrophoresis, and high performance liquid chromatography. These studies demonstrated that p-25 and gp-30 have identical protein structure, differing only by the presence of carbohydrate in gp-30. Removal of this carbohydrate by treatment with anhydrous hydrofluoric acid converted gp-30 into p-25. The NH2-terminal sequence, carboxyl-terminal sequence, and the amino acid composition of several internal tryptic peptides were found to be consistent with the proposed protein sequence based upon the published sequences of hepatitis B viral DNA. The carbohydrate of gp-30 was demonstrated to be attached within the carboxyl-terminal 104 amino acids, most likely between residues 121 and 170.
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PMID:Isolation and characterization of the major protein and glycoprotein of hepatitis B surface antigen. 724 Feb 57

Spherical hepatitis B surface antigen particles (HbsAg) of 22-nm diameter were treated with sodium dodecylsulphate in the absence of reducing agents, and their nuclei were exposed. Factors that interact with the nucleus of HbsAg were detected in the serum of HBsAg carriers who were seropositive for hepatitis B e antigen and identified as tubular forms of HBsAg. The other categories of hepatitis B antigen, Dane particles, and 22-nm spherical HBsAg did not bind with the nucleus of HBsAg. When tubular forms of HBsAg had been treated with a proteolytic enzyme, they lost the reactivity to bind with the nucleus of HBsAg. On the basis of the results obtained, tubular forms of HBsAg bear the receptor of protein nature for the nucleus of 22-nm spherical HBsAg. The receptor allows rapid determination of tubular forms by a haemagglutination method for the evaluation of their clinical and epidemiological implications.
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PMID:Tubular forms of hepatitis B surface antigen bind with the nucleus of 22-nm spherical HBsAg particles. 724 Oct 94

Protein kinase activity was found in hepatitis B virions (Dane particles) purified from the plasma of hepatitis B virus-infected patients, in virion cores, and in hepatitis B core antigen particles purified from hepatitis B virus-infected hepatic tissue and was not found in purified hepatitis B surface antigen particle preparations free of Dane particles. Only a fraction of the major polypeptide (apparent size, 19,700 daltons) in Dane particle cores and hepatitis B core antigen particles from infected liver appeared to be phosphorylated, and phosphorylation changed the electrophoretic mobility in sodium dodecyl sulfate-polyacrylamide gels to that expected for a polypeptide of 20,600 daltons. Five minor polypeptides with apparent sizes between 38,000 and 63,000 daltons were phosphorylated in Dane particles and Dane particle core preparations but were not detected in hepatitis B core antigen particles from infected liver. None of these had electrophoretic mobilities corresponding to those of known hepatitis B surface antigen polypeptides. Prolonged storage of purified hepatitis B core antigen particles or incubation with human immunoglobulin G preparations containing antibody to the hepatitis B core antigen with or without antibody to the hepatitis B e antigen resulted in the conversion of the polypeptide with an apparent size of 20,600 daltons to ones with apparent sizes of 14,700 and approximately 6,000 daltons, suggesting proteolytic cleavage of the 20,600-dalton polypeptide under these conditions.
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PMID:Protein kinase activity in hepatitis B virus. 737 11


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